HEADER TRANSFERASE 17-NOV-09 3KPV
TITLE CRYSTAL STRUCTURE OF HPNMT IN COMPLEX ADOHCY AND ADENINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHENYLETHANOLAMINE N-METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PNMTASE, NORADRENALINE N-METHYLTRANSFERASE;
COMPND 5 EC: 2.1.1.28;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PNMT, PENT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET17 PNMT-HIS
KEYWDS METHYLTRANSFERASE, FRAGMENT SCREENING, CATECHOLAMINE BIOSYNTHESIS, S-
KEYWDS 2 ADENOSYL-L-METHIONINE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.DRINKWATER,J.L.MARTIN
REVDAT 3 06-SEP-23 3KPV 1 REMARK SEQADV
REVDAT 2 01-NOV-17 3KPV 1 REMARK
REVDAT 1 29-SEP-10 3KPV 0
JRNL AUTH N.DRINKWATER,H.VU,K.M.LOVELL,K.R.CRISCIONE,B.M.COLLINS,
JRNL AUTH 2 T.E.PRISINZANO,S.A.POULSEN,M.J.MCLEISH,G.L.GRUNEWALD,
JRNL AUTH 3 J.L.MARTIN
JRNL TITL FRAGMENT-BASED SCREENING BY X-RAY CRYSTALLOGRAPHY, MS AND
JRNL TITL 2 ISOTHERMAL TITRATION CALORIMETRY TO IDENTIFY PNMT
JRNL TITL 3 (PHENYLETHANOLAMINE N-METHYLTRANSFERASE) INHIBITORS.
JRNL REF BIOCHEM.J. V. 431 51 2010
JRNL REFN ISSN 0264-6021
JRNL PMID 20642456
JRNL DOI 10.1042/BJ20100651
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.7
REMARK 3 NUMBER OF REFLECTIONS : 28505
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1432
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 45.6980 - 5.1680 0.72 2495 132 0.2090 0.2090
REMARK 3 2 5.1680 - 4.1030 0.78 2577 125 0.1950 0.2450
REMARK 3 3 4.1030 - 3.5850 0.89 2871 182 0.1910 0.2520
REMARK 3 4 3.5850 - 3.2570 0.96 3085 176 0.2110 0.2850
REMARK 3 5 3.2570 - 3.0240 0.98 3117 176 0.2310 0.3070
REMARK 3 6 3.0240 - 2.8450 0.98 3123 145 0.2210 0.2950
REMARK 3 7 2.8450 - 2.7030 0.98 3129 161 0.2140 0.3010
REMARK 3 8 2.7030 - 2.5850 0.88 2839 123 0.2210 0.3080
REMARK 3 9 2.5850 - 2.4860 0.67 2124 114 0.1990 0.3010
REMARK 3 10 2.4860 - 2.4000 0.54 1713 98 0.2010 0.2780
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 49.98
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.32600
REMARK 3 B22 (A**2) : 3.32600
REMARK 3 B33 (A**2) : -6.65200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 4284
REMARK 3 ANGLE : 0.921 5833
REMARK 3 CHIRALITY : 0.063 620
REMARK 3 PLANARITY : 0.004 759
REMARK 3 DIHEDRAL : 21.492 1581
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 24.2214 51.2977 -5.8959
REMARK 3 T TENSOR
REMARK 3 T11: 0.1804 T22: 0.0854
REMARK 3 T33: 0.1952 T12: -0.0347
REMARK 3 T13: -0.0148 T23: 0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 0.3622 L22: 0.2086
REMARK 3 L33: 0.9611 L12: -0.1074
REMARK 3 L13: 0.0101 L23: -0.2138
REMARK 3 S TENSOR
REMARK 3 S11: -0.0302 S12: 0.0124 S13: 0.0675
REMARK 3 S21: 0.0451 S22: -0.0242 S23: -0.0200
REMARK 3 S31: -0.1032 S32: 0.0212 S33: 0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3KPV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000056297.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC VARI-MAX HF
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK 9.7 W8RSSI
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28540
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 45.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.8
REMARK 200 DATA REDUNDANCY : 6.880
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 54.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.24600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MIFIT
REMARK 200 STARTING MODEL: PDB ENTRY 1HNN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6K, LICL, CACODYLATE, PH 5.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 94.40050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.08900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.08900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 141.60075
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.08900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.08900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 47.20025
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.08900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.08900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 141.60075
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.08900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.08900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 47.20025
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 94.40050
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 ALA A 4
REMARK 465 ASP A 5
REMARK 465 ARG A 6
REMARK 465 SER A 7
REMARK 465 PRO A 8
REMARK 465 ASN A 9
REMARK 465 ALA A 10
REMARK 465 GLY A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 PRO A 14
REMARK 465 ASP A 15
REMARK 465 SER A 16
REMARK 465 ALA A 17
REMARK 465 PRO A 18
REMARK 465 GLY A 19
REMARK 465 GLN A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 VAL A 23
REMARK 465 GLY A 281
REMARK 465 LEU A 282
REMARK 465 GLU A 283
REMARK 465 HIS A 284
REMARK 465 HIS A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
REMARK 465 HIS A 288
REMARK 465 HIS A 289
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 3
REMARK 465 ALA B 4
REMARK 465 ASP B 5
REMARK 465 ARG B 6
REMARK 465 SER B 7
REMARK 465 PRO B 8
REMARK 465 ASN B 9
REMARK 465 ALA B 10
REMARK 465 GLY B 11
REMARK 465 ALA B 12
REMARK 465 ALA B 13
REMARK 465 LEU B 282
REMARK 465 GLU B 283
REMARK 465 HIS B 284
REMARK 465 HIS B 285
REMARK 465 HIS B 286
REMARK 465 HIS B 287
REMARK 465 HIS B 288
REMARK 465 HIS B 289
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 82 31.25 -97.65
REMARK 500 CYS A 183 -72.39 -103.38
REMARK 500 ASP A 267 -169.05 -169.55
REMARK 500 SER B 180 116.11 -162.27
REMARK 500 CYS B 183 -63.92 -106.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADE A 290
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADE B 290
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KPJ RELATED DB: PDB
REMARK 900 RELATED ID: 3KPU RELATED DB: PDB
REMARK 900 RELATED ID: 3KPW RELATED DB: PDB
REMARK 900 RELATED ID: 3KPY RELATED DB: PDB
REMARK 900 RELATED ID: 3KQM RELATED DB: PDB
REMARK 900 RELATED ID: 3KQO RELATED DB: PDB
REMARK 900 RELATED ID: 3KQP RELATED DB: PDB
REMARK 900 RELATED ID: 3KQQ RELATED DB: PDB
REMARK 900 RELATED ID: 3KQS RELATED DB: PDB
REMARK 900 RELATED ID: 3KQT RELATED DB: PDB
REMARK 900 RELATED ID: 3KQV RELATED DB: PDB
REMARK 900 RELATED ID: 3KQW RELATED DB: PDB
REMARK 900 RELATED ID: 3KQY RELATED DB: PDB
REMARK 900 RELATED ID: 3KR0 RELATED DB: PDB
REMARK 900 RELATED ID: 3KR1 RELATED DB: PDB
REMARK 900 RELATED ID: 3KR2 RELATED DB: PDB
DBREF 3KPV A 1 282 UNP P11086 PNMT_HUMAN 1 282
DBREF 3KPV B 1 282 UNP P11086 PNMT_HUMAN 1 282
SEQADV 3KPV GLU A 283 UNP P11086 EXPRESSION TAG
SEQADV 3KPV HIS A 284 UNP P11086 EXPRESSION TAG
SEQADV 3KPV HIS A 285 UNP P11086 EXPRESSION TAG
SEQADV 3KPV HIS A 286 UNP P11086 EXPRESSION TAG
SEQADV 3KPV HIS A 287 UNP P11086 EXPRESSION TAG
SEQADV 3KPV HIS A 288 UNP P11086 EXPRESSION TAG
SEQADV 3KPV HIS A 289 UNP P11086 EXPRESSION TAG
SEQADV 3KPV GLU B 283 UNP P11086 EXPRESSION TAG
SEQADV 3KPV HIS B 284 UNP P11086 EXPRESSION TAG
SEQADV 3KPV HIS B 285 UNP P11086 EXPRESSION TAG
SEQADV 3KPV HIS B 286 UNP P11086 EXPRESSION TAG
SEQADV 3KPV HIS B 287 UNP P11086 EXPRESSION TAG
SEQADV 3KPV HIS B 288 UNP P11086 EXPRESSION TAG
SEQADV 3KPV HIS B 289 UNP P11086 EXPRESSION TAG
SEQRES 1 A 289 MET SER GLY ALA ASP ARG SER PRO ASN ALA GLY ALA ALA
SEQRES 2 A 289 PRO ASP SER ALA PRO GLY GLN ALA ALA VAL ALA SER ALA
SEQRES 3 A 289 TYR GLN ARG PHE GLU PRO ARG ALA TYR LEU ARG ASN ASN
SEQRES 4 A 289 TYR ALA PRO PRO ARG GLY ASP LEU CYS ASN PRO ASN GLY
SEQRES 5 A 289 VAL GLY PRO TRP LYS LEU ARG CYS LEU ALA GLN THR PHE
SEQRES 6 A 289 ALA THR GLY GLU VAL SER GLY ARG THR LEU ILE ASP ILE
SEQRES 7 A 289 GLY SER GLY PRO THR VAL TYR GLN LEU LEU SER ALA CYS
SEQRES 8 A 289 SER HIS PHE GLU ASP ILE THR MET THR ASP PHE LEU GLU
SEQRES 9 A 289 VAL ASN ARG GLN GLU LEU GLY ARG TRP LEU GLN GLU GLU
SEQRES 10 A 289 PRO GLY ALA PHE ASN TRP SER MET TYR SER GLN HIS ALA
SEQRES 11 A 289 CYS LEU ILE GLU GLY LYS GLY GLU CYS TRP GLN ASP LYS
SEQRES 12 A 289 GLU ARG GLN LEU ARG ALA ARG VAL LYS ARG VAL LEU PRO
SEQRES 13 A 289 ILE ASP VAL HIS GLN PRO GLN PRO LEU GLY ALA GLY SER
SEQRES 14 A 289 PRO ALA PRO LEU PRO ALA ASP ALA LEU VAL SER ALA PHE
SEQRES 15 A 289 CYS LEU GLU ALA VAL SER PRO ASP LEU ALA SER PHE GLN
SEQRES 16 A 289 ARG ALA LEU ASP HIS ILE THR THR LEU LEU ARG PRO GLY
SEQRES 17 A 289 GLY HIS LEU LEU LEU ILE GLY ALA LEU GLU GLU SER TRP
SEQRES 18 A 289 TYR LEU ALA GLY GLU ALA ARG LEU THR VAL VAL PRO VAL
SEQRES 19 A 289 SER GLU GLU GLU VAL ARG GLU ALA LEU VAL ARG SER GLY
SEQRES 20 A 289 TYR LYS VAL ARG ASP LEU ARG THR TYR ILE MET PRO ALA
SEQRES 21 A 289 HIS LEU GLN THR GLY VAL ASP ASP VAL LYS GLY VAL PHE
SEQRES 22 A 289 PHE ALA TRP ALA GLN LYS VAL GLY LEU GLU HIS HIS HIS
SEQRES 23 A 289 HIS HIS HIS
SEQRES 1 B 289 MET SER GLY ALA ASP ARG SER PRO ASN ALA GLY ALA ALA
SEQRES 2 B 289 PRO ASP SER ALA PRO GLY GLN ALA ALA VAL ALA SER ALA
SEQRES 3 B 289 TYR GLN ARG PHE GLU PRO ARG ALA TYR LEU ARG ASN ASN
SEQRES 4 B 289 TYR ALA PRO PRO ARG GLY ASP LEU CYS ASN PRO ASN GLY
SEQRES 5 B 289 VAL GLY PRO TRP LYS LEU ARG CYS LEU ALA GLN THR PHE
SEQRES 6 B 289 ALA THR GLY GLU VAL SER GLY ARG THR LEU ILE ASP ILE
SEQRES 7 B 289 GLY SER GLY PRO THR VAL TYR GLN LEU LEU SER ALA CYS
SEQRES 8 B 289 SER HIS PHE GLU ASP ILE THR MET THR ASP PHE LEU GLU
SEQRES 9 B 289 VAL ASN ARG GLN GLU LEU GLY ARG TRP LEU GLN GLU GLU
SEQRES 10 B 289 PRO GLY ALA PHE ASN TRP SER MET TYR SER GLN HIS ALA
SEQRES 11 B 289 CYS LEU ILE GLU GLY LYS GLY GLU CYS TRP GLN ASP LYS
SEQRES 12 B 289 GLU ARG GLN LEU ARG ALA ARG VAL LYS ARG VAL LEU PRO
SEQRES 13 B 289 ILE ASP VAL HIS GLN PRO GLN PRO LEU GLY ALA GLY SER
SEQRES 14 B 289 PRO ALA PRO LEU PRO ALA ASP ALA LEU VAL SER ALA PHE
SEQRES 15 B 289 CYS LEU GLU ALA VAL SER PRO ASP LEU ALA SER PHE GLN
SEQRES 16 B 289 ARG ALA LEU ASP HIS ILE THR THR LEU LEU ARG PRO GLY
SEQRES 17 B 289 GLY HIS LEU LEU LEU ILE GLY ALA LEU GLU GLU SER TRP
SEQRES 18 B 289 TYR LEU ALA GLY GLU ALA ARG LEU THR VAL VAL PRO VAL
SEQRES 19 B 289 SER GLU GLU GLU VAL ARG GLU ALA LEU VAL ARG SER GLY
SEQRES 20 B 289 TYR LYS VAL ARG ASP LEU ARG THR TYR ILE MET PRO ALA
SEQRES 21 B 289 HIS LEU GLN THR GLY VAL ASP ASP VAL LYS GLY VAL PHE
SEQRES 22 B 289 PHE ALA TRP ALA GLN LYS VAL GLY LEU GLU HIS HIS HIS
SEQRES 23 B 289 HIS HIS HIS
HET SAH A2001 26
HET ADE A 290 10
HET SAH B2002 26
HET ADE B 290 10
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM ADE ADENINE
FORMUL 3 SAH 2(C14 H20 N6 O5 S)
FORMUL 4 ADE 2(C5 H5 N5)
FORMUL 7 HOH *207(H2 O)
HELIX 1 1 SER A 25 ARG A 29 5 5
HELIX 2 2 GLU A 31 ALA A 41 1 11
HELIX 3 3 GLY A 52 THR A 67 1 16
HELIX 4 4 VAL A 84 LEU A 88 5 5
HELIX 5 5 SER A 89 PHE A 94 5 6
HELIX 6 6 LEU A 103 GLN A 115 1 13
HELIX 7 7 TRP A 123 GLY A 135 1 13
HELIX 8 8 CYS A 139 ARG A 150 1 12
HELIX 9 9 CYS A 183 SER A 188 5 6
HELIX 10 10 ASP A 190 THR A 203 1 14
HELIX 11 11 SER A 235 SER A 246 1 12
HELIX 12 12 PRO A 259 GLN A 263 5 5
HELIX 13 13 SER B 16 GLN B 28 1 13
HELIX 14 14 GLU B 31 ALA B 41 1 11
HELIX 15 15 GLY B 52 THR B 67 1 16
HELIX 16 16 VAL B 84 LEU B 88 5 5
HELIX 17 17 SER B 89 PHE B 94 5 6
HELIX 18 18 LEU B 103 GLN B 115 1 13
HELIX 19 19 TRP B 123 GLY B 135 1 13
HELIX 20 20 CYS B 139 ARG B 150 1 12
HELIX 21 21 CYS B 183 SER B 188 1 6
HELIX 22 22 ASP B 190 THR B 203 1 14
HELIX 23 23 SER B 235 GLY B 247 1 13
HELIX 24 24 PRO B 259 GLN B 263 5 5
SHEET 1 A 7 VAL A 151 LEU A 155 0
SHEET 2 A 7 ASP A 96 THR A 100 1 N MET A 99 O LEU A 155
SHEET 3 A 7 THR A 74 ILE A 78 1 N ASP A 77 O THR A 98
SHEET 4 A 7 ALA A 175 ALA A 181 1 O VAL A 179 N ILE A 78
SHEET 5 A 7 LEU A 205 LEU A 217 1 O HIS A 210 N LEU A 178
SHEET 6 A 7 GLY A 271 LYS A 279 -1 O ALA A 277 N LEU A 211
SHEET 7 A 7 TYR A 248 ILE A 257 -1 N TYR A 256 O VAL A 272
SHEET 1 B 2 TRP A 221 ALA A 224 0
SHEET 2 B 2 ALA A 227 THR A 230 -1 O ALA A 227 N ALA A 224
SHEET 1 C 7 VAL B 151 LEU B 155 0
SHEET 2 C 7 ASP B 96 THR B 100 1 N MET B 99 O LEU B 155
SHEET 3 C 7 THR B 74 ASP B 77 1 N ASP B 77 O THR B 98
SHEET 4 C 7 ALA B 175 ALA B 181 1 O VAL B 179 N ILE B 76
SHEET 5 C 7 LEU B 205 LEU B 217 1 O HIS B 210 N LEU B 178
SHEET 6 C 7 GLY B 271 LYS B 279 -1 O ALA B 275 N LEU B 213
SHEET 7 C 7 TYR B 248 ILE B 257 -1 N ASP B 252 O TRP B 276
SHEET 1 D 2 TRP B 221 ALA B 224 0
SHEET 2 D 2 ALA B 227 THR B 230 -1 O ALA B 227 N ALA B 224
SSBOND 1 CYS A 48 CYS B 139 1555 1555 2.04
SSBOND 2 CYS A 139 CYS B 48 1555 1555 2.04
CISPEP 1 PRO A 42 PRO A 43 0 -1.45
CISPEP 2 LEU A 173 PRO A 174 0 -0.99
CISPEP 3 PRO B 42 PRO B 43 0 2.38
CISPEP 4 LEU B 173 PRO B 174 0 -5.25
SITE 1 AC1 20 TYR A 27 TYR A 35 TYR A 40 GLY A 79
SITE 2 AC1 20 SER A 80 GLY A 81 THR A 83 TYR A 85
SITE 3 AC1 20 ASP A 101 PHE A 102 LEU A 103 ASN A 106
SITE 4 AC1 20 ILE A 157 ASP A 158 VAL A 159 HIS A 160
SITE 5 AC1 20 ALA A 181 PHE A 182 CYS A 183 VAL A 187
SITE 1 AC2 22 TYR B 27 TYR B 35 TYR B 40 GLY B 79
SITE 2 AC2 22 SER B 80 GLY B 81 THR B 83 TYR B 85
SITE 3 AC2 22 ASP B 101 PHE B 102 LEU B 103 ASN B 106
SITE 4 AC2 22 ASP B 158 VAL B 159 HIS B 160 ALA B 181
SITE 5 AC2 22 PHE B 182 CYS B 183 VAL B 187 HOH B2015
SITE 6 AC2 22 HOH B2101 HOH B2197
SITE 1 AC3 12 TYR A 35 ASN A 39 TYR A 40 ARG A 44
SITE 2 AC3 12 PHE A 182 GLU A 219 TYR A 222 ASP A 267
SITE 3 AC3 12 HOH A2232 HOH A2233 HOH A2235 HOH A2237
SITE 1 AC4 11 TYR B 35 ASN B 39 TYR B 40 ARG B 44
SITE 2 AC4 11 PHE B 182 GLU B 219 TYR B 222 ASP B 267
SITE 3 AC4 11 HOH B2101 HOH B2244 HOH B2245
CRYST1 94.178 94.178 188.801 90.00 90.00 90.00 P 43 21 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010618 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005297 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
